PTC3_CAEEL
ID PTC3_CAEEL Reviewed; 1367 AA.
AC H2L0G5; H2L0G4; Q6AW16;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Protein patched homolog 3 {ECO:0000305};
GN Name=ptc-3 {ECO:0000312|WormBase:Y110A2AL.8c};
GN ORFNames=Y110A2AL.8 {ECO:0000312|WormBase:Y110A2AL.8c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-706 AND ASP-789.
RX PubMed=21215260; DOI=10.1016/j.ydbio.2010.12.035;
RA Soloviev A., Gallagher J., Marnef A., Kuwabara P.E.;
RT "C. elegans patched-3 is an essential gene implicated in osmoregulation and
RT requiring an intact permease transporter domain.";
RL Dev. Biol. 351:242-253(2011).
CC -!- FUNCTION: Regulates osmosis during embryonic development. Required for
CC larval development and in particular is involved in larval molting.
CC {ECO:0000269|PubMed:21215260}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:21215260}; Multi-pass membrane protein
CC {ECO:0000255}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:21215260}. Note=Co-localizes with ajm-1, an
CC adherens junction marker in hypodermal cells and vulval toroids.
CC {ECO:0000269|PubMed:21215260}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:Y110A2AL.8c};
CC IsoId=H2L0G5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y110A2AL.8a};
CC IsoId=H2L0G5-2; Sequence=VSP_058384;
CC Name=b {ECO:0000312|WormBase:Y110A2AL.8b};
CC IsoId=H2L0G5-3; Sequence=VSP_058384, VSP_058385;
CC -!- TISSUE SPECIFICITY: In males, expressed in the precursor and mature
CC sensory rays, the cloaca, and pre-anal ganglia and cephalic neurons.
CC Also expressed in five cells in the valve region between the seminal
CC vesicle and vas deferens of the somatic gonad.
CC {ECO:0000269|PubMed:21215260}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the hypodermis of embryos prior to
CC hatching and expression is enhanced in the hypodermis before each molt.
CC Expressed during larval development in the excretory duct at the L1
CC stage, and during morphogenesis of the somatic gonad and vulva during
CC the L3 and L4 stages with prominent expression in the uterine seam cell
CC and toroidal vulE and vulD cells. {ECO:0000269|PubMed:21215260}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with embryos displaying a fluid-
CC filled appearance and dying at hatching. RNAi-mediated knockdown
CC results in high levels of embryonic and larval lethality. Dead and
CC dying mutants do not respond to touch, display extensive vacuolation,
CC molting defects which include unshed cuticles and in particular male
CC specific molting defects that prevent unfurling of the mature tail
CC rays. Surviving mutants are shorter in length and display defective
CC egg-laying and abnormal vulval morphogenesis.
CC {ECO:0000269|PubMed:21215260}.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; BX284602; CCD72983.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD72978.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD72979.1; -; Genomic_DNA.
DR RefSeq; NP_001122650.1; NM_001129178.1. [H2L0G5-1]
DR RefSeq; NP_494383.2; NM_061982.5. [H2L0G5-3]
DR RefSeq; NP_494384.2; NM_061983.6. [H2L0G5-2]
DR AlphaFoldDB; H2L0G5; -.
DR SMR; H2L0G5; -.
DR STRING; 6239.Y110A2AL.8c; -.
DR EPD; H2L0G5; -.
DR PaxDb; H2L0G5; -.
DR PeptideAtlas; H2L0G5; -.
DR EnsemblMetazoa; Y110A2AL.8a.1; Y110A2AL.8a.1; WBGene00004210. [H2L0G5-2]
DR EnsemblMetazoa; Y110A2AL.8b.1; Y110A2AL.8b.1; WBGene00004210. [H2L0G5-3]
DR EnsemblMetazoa; Y110A2AL.8c.1; Y110A2AL.8c.1; WBGene00004210. [H2L0G5-1]
DR GeneID; 173631; -.
DR KEGG; cel:CELE_Y110A2AL.8; -.
DR UCSC; Y110A2AL.8a; c. elegans.
DR CTD; 173631; -.
DR WormBase; Y110A2AL.8a; CE37163; WBGene00004210; ptc-3. [H2L0G5-2]
DR WormBase; Y110A2AL.8b; CE37164; WBGene00004210; ptc-3. [H2L0G5-3]
DR WormBase; Y110A2AL.8c; CE42182; WBGene00004210; ptc-3. [H2L0G5-1]
DR eggNOG; KOG1935; Eukaryota.
DR InParanoid; H2L0G5; -.
DR OMA; DFISAQF; -.
DR OrthoDB; 1190129at2759; -.
DR PhylomeDB; H2L0G5; -.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR PRO; PR:H2L0G5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004210; Expressed in larva and 3 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097108; F:hedgehog family protein binding; IBA:GO_Central.
DR GO; GO:0008158; F:hedgehog receptor activity; IBA:GO_Central.
DR GO; GO:0005119; F:smoothened binding; IBA:GO_Central.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF02460; Patched; 2.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1367
FT /note="Protein patched homolog 3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436535"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..625
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..767
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 885..1143
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1193..1199
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1200..1220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1221..1237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1259..1273
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1274..1294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1295..1367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 627..788
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1301..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 2..28
FT /note="SFPDEETDLLSEAKHCIRNVIHRTHRK -> KVHSEQPPGKDEPGPIRR
FT (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058384"
FT VAR_SEQ 822
FT /note="N -> NNTQ (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058385"
FT MUTAGEN 706
FT /note="D->A: No obvious phenotype."
FT /evidence="ECO:0000269|PubMed:21215260"
FT MUTAGEN 789
FT /note="D->N: Rescues lethality of the null mutant."
FT /evidence="ECO:0000269|PubMed:21215260"
SQ SEQUENCE 1367 AA; 153280 MW; E3810D73321719CB CRC64;
MSFPDEETDL LSEAKHCIRN VIHRTHRKFL ENRLIGNFDS EDFSDAWKKK FAHAPTWCDA
DMSLQQIKRG KAVGNTVALT ARAFFQLWLF RIGCFVQRWA WSTIFISLFL YCLCLGGLRH
VTIETDLVKL WVSEGGRLNE EMGYLGQVKF ERESGHLVHK VKRAVEQTTE PPAPAVKAEV
RRGPELPKEN GLGGGFQVVI QTPSFDGQNI LSKEALQQHT KLMEEISTYE VKMFNETWTL
SDICFKPPGP SFNSGPLAGI MSKLLDKIIP CIWITPIDCY WDGAKPLGPN PPLNLGPEVA
SFVSSLPPGN VTWKNLNPTS VIKEVGTLFD LGPIGNFFER AGIDGAYLDR PCIDPLEEEC
PKSAPNYFDR CHALTKFNEW NMAKAMSEQV TLERKIIPKD DGKSDIAETI LNDIFGKKRR
KRQADTTTKK PATKKDEDYY EYEDDADYLA GIANSTIAKK NPEKEAKDLL CLEYGSSLLK
WMQENPERLG EFLTKEEMPD YPNYGDVMTG GCKGFGKKIM EWPEDLIIGG IQRDNGKLVS
AEALQSVFLV SGAYDVFARI KNDKTDSHPG LDRHHFQPWM AGEIISTWQR NFTKRLYSHE
LNRERRQFHP LASTSIADML EEFSQFNYII IVIGYILMVI YAAFTQGRFQ GWWLAVQSNV
ALAICGVILV TISSICGLGF ATHLGINFNA ATTQVVPFLS LGLGIDDMFL LLHNYDEIIN
ICNKNEIGVL LKETGMSVML TSINNILAFI SGYVLPIPAL RSFCSQTAIL LAFNLIFLMF
IFPAMIGIDL RRQRKGKRDL AYCSRGNPQM ATSQSVPSNV SNMSSRAELA GYEKQADEYK
RHEPWYTVGG FLNKIYIPAL KNNVVKACVL IGTTTAVVFG LYGMYTSTLG LELADVLPEH
TPPAAFLRAR EQYFSFYPMF AVLRGDKLDI PNQQQLIEEY RAQLGSSKFM IKAEGKLQPY
WMSMLRVWLQ SLDMALEKDL AAGKFDLTNG NPIKVNGEKP SPESMIAARL VCSFGTNYNC
DGRLGKMKMV ENEVINPEGF YNYLTGWFNV DNMMYYVSQA SFYPTPPGWE YNEKLAKVVP
AAEPLLYSQM PFYQNDLIDT PAIVKMIEEI RATCEEYSER GLSNHPSGIA FTFWEQYLTL
RWNLFQAICI IALAVFCVIS ILMFNPWAAT LIMCIVVITT IELGGFMGLM GIKMNPISAV
TLICAVGIGV EFTAHVELAF LTALGTIDQR LESCLQHMFV PVYHGAISTF LGVVMLVFSE
FDFVVTYFFY TMTLLVALGV FNGLCVLPVI LTLVGPKPEL TPTDGSSVLP PPPPLRQQYA
EKSGGVEGGM RKRKEKRPAE VEMSARDSPS TSSASHSSDD ESSPAHK
